6O57
Crystal Structure of multi-drug resistant HIV-1 protease PR-S17 with a substrate analog p2-NC in P41
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-02-28 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 41 |
| Unit cell lengths | 54.881, 54.881, 82.131 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.460 - 1.710 |
| R-factor | 0.19984 |
| Rwork | 0.198 |
| R-free | 0.23100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sgu |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.206 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0222) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.770 |
| High resolution limit [Å] | 1.710 | 1.710 |
| Rmerge | 0.071 | 0.471 |
| Rpim | 0.031 | 0.280 |
| Number of reflections | 26117 | 2508 |
| <I/σ(I)> | 21.2 | 2.6 |
| Completeness [%] | 99.1 | 95.2 |
| Redundancy | 6.1 | 3.4 |
| CC(1/2) | 0.817 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 29.5% PEG 4000, 0.2M ammonium acetate and 0.1M sodium acetate buffer at pH 4.6 |
